Inhibition in multicopper oxidases: a critical review

Valles, Morgane; Kamaruddin, Amirah Farhan; Wong, Lu Shin; Blanford, Christopher F.

doi:10.1039/d0cy00724b

Cited by 25 publications

(30 citation statements)

References 301 publications

(396 reference statements)

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“…Issues in the communication of the enzyme with the electrode, inappropriate redox potential or chloride sensitivity impose to search for more efficient redox enzymes for O2 reduction [8,11].…”

Section: Introductionmentioning

confidence: 99%

Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus

et al. 2021

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Thermus thermophilus laccase belongs to the sub-class of multicopper oxidases that is activated by the extra binding of copper to a methionine-rich domain allowing an electron pathway from the substrate to the conventional first electron acceptor, the T1 Cu. In this work, two key amino acid residues in the 1 st and 2 nd coordination spheres of T1 Cu are mutated in view of tuning their redox potential and investigating their influence on copper-related activity. Evolution of the kinetic parameters after copper addition highlights that both mutations play a key role influencing the enzymatic activity in distinct unexpected ways. These results clearly indicate that the methionine rich domain is not the only actor in the cuprous oxidase activity of CueO-like enzymes.

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Section: Introductionmentioning

confidence: 99%

Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus

et al. 2021

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“…BODs are considered to preserve their enzymatic activity in the presence of Cl À [26]. However, it has been indicated that the presence of chloride ions can also alter the oxidative state of BOD, which leads to a decrease in their activity [45,46]. As shown in Figure 5, after addition of CaCl 2 to the electrolyte solution the catalytic current at the biocathode decreased significantly and reached similar current values as those observed for the bioanode.…”

Section: Biofuel Cell Characterizationmentioning

confidence: 69%

Assembling a Low‐volume Biofuel Cell on a Screen‐printed Electrode for Glucose Sensing

et al. 2022

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An enzymatic biofuel cell is integrated on a screen-printed electrode as a basis for a self-powered biosensor. A glucose/O 2 biofuel cell consisting of a pyrroloquinoline quinone-dependent glucose dehydrogenase embedded within an Os-complex modified redox polymer bioanode to oxidize glucose and a non-limiting bilirubin oxidase-based gas diffusion biocathode in the direct-electron transfer regime for the reduction of O 2 showed a glucose-dependent current and power output. For full integration on a single screen-printed electrode, a miniaturized agar salt bridge was introduced between the two bioelectrodes to ensure operation of the assembly in a two-compartment configuration with each electrode operating at optimal conditions.

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“…In the Mr laccase molecule, both T2 and T1/T3α channels were structurally combined in the T2/T3 center, which corresponds to the catalytic reaction mechanism. [43] Comparison of the amino acid composition of the studied Mr laccase and the laccases of a known structure showed the…”

Section: Structure Analysis Of the Laccase Of M Roridum Vkm F-3565mentioning

confidence: 99%

The Laccase of Myrothecium roridum VKM F‐3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions**

et al. 2023

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Most of the currently known fungal laccases show their maximum activity under acidic environmental conditions. It is known that a decrease in the activity of a typical laccase at neutral or alkaline pH values is the result of an increase in the binding of the hydroxide anion to the T2/T3 copper center, which prevents the transfer of an electron from the T1 Cu to the trinuclear copper center. However, evolutionary pressure has resolved the existing limitations in the catalytic mechanism of laccase, allowing such enzymes to be functionally active under neutral/alkaline pH conditions, thereby giving fungi an advantage for their survival. Combined molecular and biochemical studies, homological modeling, calculation of the electrostatic potential on the Connolly surface at pH 5.0 and 7.0, and structural analysis of the novel alkaliphilic laccase of Myrothecium roridum VKM F‐3565 and alkaliphilic and acidophilic fungal laccases with a known structure allowed a new intramolecular channel near the one of the catalytic aspartate residues at T2‐copper atom to be found. The amino acid residues of alkaliphilic laccases forming this channel can presumably serve as proton donors for catalytic aspartates under neutral conditions, thus ensuring proper functioning. For the first time for ascomycetous laccases, the production of new trimeric products of phenylpropanoid condensation under neutral conditions has been shown, which could have a potential for use in pharmacology.

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Inhibition in multicopper oxidases: a critical review

Abstract: Multicopper oxidases (MCO), such as laccases and bilirubin oxidases, are catalysts of wide interest to a range of biotechnological applications, especially bioremediation and energy transduction. Many of these processes take...

Cited by 25 publications

References 301 publications

Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus

Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus

Assembling a Low‐volume Biofuel Cell on a Screen‐printed Electrode for Glucose Sensing

The Laccase of Myrothecium roridum VKM F‐3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions**

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